ArticleJournal of enzyme inhibition and medicinal chemistry2019
Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach.
Article in Journal of enzyme inhibition and medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- 4-Cyanamidobenzenesulfonamide derivatives: a novel class of human and bacterial carbonic anhydrase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Investigation of novel alkyl/benzyl (4-sulphamoylphenyl)carbamimidothioates as carbonic anhydrase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Intrinsically disordered features of carbonic anhydrase IX proteoglycan-like domain.Cellular and molecular life sciences : CMLS · 2021Review
- Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
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7 authors.
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Abstract
Carbonic anhydrases (CAs) are ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide to bicarbonate and proton. In humans there are 15 isoforms among which only 12 are catalytically active. Since active human (h) CAs show different efficiency, the understanding of the molecular determinants affecting it is a matter of debate. Here we investigated, by a site-specific mutagenesis approach, residues modulating the catalytic features of one of the least investigated cytosolic isoform, i.e. hCA XIII. Results showed that residues assisting the formation of an ordered solvent network within the catalytic site as well as those forming a histidine cluster on the protein surface are important to guarantee an efficient proton transfer.
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